Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P).
A novel human cDNA (XPNPEPL) encoding a protein of 623 amino acids exhibiting 44% sequence identity and 62% sequence similarity to pig kidney X-prolyl aminopeptidase (aminopeptidase P; EC 3.4.11.9) was obtained by reverse transcription/polymerase chain reaction of phytohemagglutinin-stimulated lymphocyte mRNA. Conserved sequences were found with the prokaryotic X-prolyl aminopeptidase encoding gene (pepP). The human gene translation product exhibits a high sequence homology to the Schizosaccharomyces pombe chromosome I hypothetical protein C22G7.01c and to the S. cerevisiae ORF y11029w. Northern blot analysis indicates an ubiquitous expression of the human XPNPEPL sequence.
Vanhoof
G
G
Department of Clinical Biochemistry, University of Antwerp, Wilrijk, Belgium. gvhoof@uia.ua.ac.be
Goossens
F
F
Juliano
M A
MA
Juliano
L
L
Hendriks
D
D
Schatteman
K
K
Lin
A H
AH
Scharpé
S
S
D000626:Aminopeptidases / Q000235:genetics*; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D017124:Conserved Sequence; D017931:DNA Primers; D018076:DNA, Complementary; D006801:Humans; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000032:analysis; D017386:Sequence Homology, Amino Acid; D013552:Swine
D017931:DNA Primers; D018076:DNA, Complementary; D012333:RNA, Messenger; D000626:Aminopeptidases; C022750:X-Pro aminopeptidase